https://scholars.lib.ntu.edu.tw/handle/123456789/624882
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.author | Chang Y.-M | en_US |
dc.contributor.author | Ho C.-H | en_US |
dc.contributor.author | Chen C.K.-M | en_US |
dc.contributor.author | MANUEL MAESTRE-REYNA | en_US |
dc.contributor.author | Chang-Chien M.W | en_US |
dc.contributor.author | Wang A.H.-J. | en_US |
dc.creator | Chang Y.-M;Ho C.-H;Chen C.K.-M;Maestre-Reyna M;Chang-Chien M.W;Wang A.H.-J. | - |
dc.date.accessioned | 2022-11-11T03:00:21Z | - |
dc.date.available | 2022-11-11T03:00:21Z | - |
dc.date.issued | 2014 | - |
dc.identifier.issn | 03051048 | - |
dc.identifier.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84899823502&doi=10.1093%2fnar%2fgku128&partnerID=40&md5=51f36b37554b6b0dc1dffb65e1939cdd | - |
dc.identifier.uri | https://scholars.lib.ntu.edu.tw/handle/123456789/624882 | - |
dc.description.abstract | The teicoplanin-associated locus regulator (TcaR) regulates gene expression of proteins on the intercellular adhesion (ica) locus involved in staphylococci poly-N-acetylglucosamine biosynthesis. The absence of TcaR increases poly-N-acetylglucosamine production and promotes biofilm formation. Until recently, the mechanism of multiple antibiotic resistance regulator family protein members, such as TcaR, was restricted to binding double-stranded DNA. However, we recently found that TcaR strongly interacts with single-stranded DNA, which is a new role for this family of proteins. In this study, we report Staphylococcus epidermidis TcaR-single-stranded DNA complex structures. Our model suggests that TcaR and single-stranded DNA form a 61-symmetry polymer composed of TcaR dimers with single-stranded DNA that wraps outside the polymer and 12 nt per TcaR dimer. Single-stranded DNA binding to TcaR involves a large conformational change at the DNA binding lobe. Several point mutations involving the single-stranded DNA binding surface validate interactions between single-stranded DNA and TcaR. Our results extend the novel role of multiple antibiotic resistance regulator family proteins in staphylococci. © 2014 © The Author(s) 2014. Published by Oxford University Press. | - |
dc.relation.ispartof | Nucleic Acids Research | - |
dc.subject.other | bacterial protein; multidrug resistance protein; single stranded DNA; teicoplanin associated locus regulator; unclassified drug; article; binding site; conformational transition; controlled study; crystal structure; DNA structure; gene expression; nonhuman; point mutation; priority journal; protein DNA binding; protein DNA interaction; protein expression; protein function; protein structure; regulatory mechanism; Staphylococcus epidermidis; Bacterial Proteins; Crystallography, X-Ray; DNA, Single-Stranded; DNA-Binding Proteins; Models, Molecular; Protein Binding; Staphylococcus epidermidis | - |
dc.title | TcaR-ssDNA complex crystal structure reveals new DNA binding mechanism of the MarR family proteins | en_US |
dc.type | journal article | en |
dc.identifier.doi | 10.1093/nar/gku128 | - |
dc.identifier.pmid | 24531929 | - |
dc.identifier.scopus | 2-s2.0-84899823502 | - |
dc.relation.pages | 5314-5321 | - |
dc.relation.journalvolume | 42 | - |
dc.relation.journalissue | 8 | - |
item.openairetype | journal article | - |
item.openairecristype | http://purl.org/coar/resource_type/c_6501 | - |
item.fulltext | no fulltext | - |
item.grantfulltext | none | - |
item.cerifentitytype | Publications | - |
crisitem.author.dept | Chemistry | - |
crisitem.author.orcid | 0000-0002-9566-7216 | - |
crisitem.author.parentorg | College of Science | - |
顯示於: | 化學系 |
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